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O00418

- EF2K_HUMAN

UniProt

O00418 - EF2K_HUMAN

Protein

Eukaryotic elongation factor 2 kinase

Gene

EEF2K

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 2 (28 Jul 2009)
      Previous versions | rss
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    Functioni

    Threonine kinase that regulates protein synthesis by controlling the rate of peptide chain elongation. Upon activation by a variety of upstream kinases including AMPK or TRPM7, phosphorylates the elongation factor EEF2 at a single site, renders it unable to bind ribosomes and thus inactive. In turn, the rate of protein synthesis is reduced.2 Publications

    Catalytic activityi

    ATP + [elongation factor 2] = ADP + [elongation factor 2] phosphate.1 Publication

    Enzyme regulationi

    Undergoes calcium/calmodulin-dependent intramolecular autophosphorylation, and this results in it becoming partially calcium/calmodulin-independent.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi296 – 3027ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. calcium ion binding Source: InterPro
    3. calmodulin binding Source: UniProtKB
    4. elongation factor-2 kinase activity Source: UniProtKB
    5. protein kinase activity Source: ProtInc
    6. translation factor activity, nucleic acid binding Source: ProtInc

    GO - Biological processi

    1. insulin receptor signaling pathway Source: Reactome
    2. protein autophosphorylation Source: UniProtKB
    3. regulation of protein autophosphorylation Source: Ensembl
    4. translational elongation Source: ProtInc

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.20. 2681.
    ReactomeiREACT_6772. S6K1 signalling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Eukaryotic elongation factor 2 kinase (EC:2.7.11.20)
    Short name:
    eEF-2 kinase
    Short name:
    eEF-2K
    Alternative name(s):
    Calcium/calmodulin-dependent eukaryotic elongation factor 2 kinase
    Gene namesi
    Name:EEF2K
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

    Organism-specific databases

    HGNCiHGNC:24615. EEF2K.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi78 – 781S → A: Decreased kinase activity. 1 Publication
    Mutagenesisi348 – 3481T → A: Decreased kinase activity. 1 Publication
    Mutagenesisi366 – 3661S → A: Abrogates phosphorylation by RPS6KB1. 2 Publications
    Mutagenesisi366 – 3661S → A: Decreased kinase activity. 2 Publications

    Organism-specific databases

    PharmGKBiPA134992891.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 725724Eukaryotic elongation factor 2 kinasePRO_0000086936Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei18 – 181Phosphoserine6 Publications
    Modified residuei61 – 611Phosphoserine; by autocatalysis1 Publication
    Modified residuei66 – 661Phosphoserine; by autocatalysis1 Publication
    Modified residuei71 – 711PhosphoserineBy similarity
    Modified residuei78 – 781Phosphoserine; by autocatalysis and TRPM72 Publications
    Modified residuei348 – 3481Phosphothreonine; by autocatalysis3 Publications
    Modified residuei353 – 3531Phosphothreonine; by autocatalysis1 Publication
    Modified residuei359 – 3591Phosphoserine; by MAPK13 and CDK12 Publications
    Modified residuei366 – 3661Phosphoserine; by autocatalysis, RPS6KA1 and RPS6KB12 Publications
    Modified residuei398 – 3981Phosphoserine; by AMPK1 Publication
    Modified residuei445 – 4451Phosphoserine; by autocatalysis3 Publications
    Modified residuei470 – 4701Phosphoserine3 Publications
    Modified residuei474 – 4741Phosphoserine; by autocatalysis4 Publications
    Modified residuei477 – 4771Phosphoserine1 Publication
    Modified residuei491 – 4911Phosphoserine; by autocatalysis1 Publication
    Modified residuei500 – 5001Phosphoserine; by PKABy similarity

    Post-translational modificationi

    Autophosphorylated at multiple residues, Thr-348 being the major site. Phosphorylated by AMP-activated protein kinase AMPK at Ser-398 leading to EEF2K activation and protein synthesis inhibition. Phosphorylated by TRPM7 at Ser-78 resulting in improved protein stability, higher EE2F phosphorylated and subsequently reduced rate of protein synthesis. Phosphorylation by other kinases such as CDK1 and MAPK13 at Ser-359 or RPS6KA1 and RPS6KB1 at Ser-366 instead decrease EEF2K activity and promote protein synthesis.13 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO00418.
    PaxDbiO00418.
    PRIDEiO00418.

    PTM databases

    PhosphoSiteiO00418.

    Expressioni

    Gene expression databases

    ArrayExpressiO00418.
    BgeeiO00418.
    CleanExiHS_EEF2K.
    GenevestigatoriO00418.

    Organism-specific databases

    HPAiCAB007818.

    Interactioni

    Subunit structurei

    Monomer or homodimer.Curated

    Protein-protein interaction databases

    BioGridi118953. 33 interactions.
    IntActiO00418. 10 interactions.
    MINTiMINT-207181.
    STRINGi9606.ENSP00000263026.

    Structurei

    3D structure databases

    ProteinModelPortaliO00418.
    SMRiO00418. Positions 117-323, 527-645.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini116 – 326211Alpha-type protein kinasePROSITE-ProRule annotationsAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni594 – 61017Calmodulin-bindingSequence AnalysisAdd
    BLAST
    Regioni610 – 62718Pseudosubstrate/autoinhibitory domainSequence AnalysisAdd
    BLAST

    Domaini

    The catalytic domain is located to N-terminal region. The neighbor region contains the calmodulin-binding domain.1 Publication

    Sequence similaritiesi

    Contains 1 alpha-type protein kinase domain.PROSITE-ProRule annotations

    Phylogenomic databases

    eggNOGiNOG145133.
    HOGENOMiHOG000022023.
    HOVERGENiHBG002318.
    InParanoidiO00418.
    KOiK08292.
    OMAiQIHTETG.
    OrthoDBiEOG7673B0.
    PhylomeDBiO00418.
    TreeFamiTF316085.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    InterProiIPR017400. Elongation_factor_2_kinase.
    IPR011009. Kinase-like_dom.
    IPR004166. MHCK_EF2_kinase.
    IPR006597. Sel1-like.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF02816. Alpha_kinase. 1 hit.
    PF08238. Sel1. 4 hits.
    [Graphical view]
    PIRSFiPIRSF038139. Elongation_factor_2_kinase. 1 hit.
    SMARTiSM00811. Alpha_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51158. ALPHA_KINASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O00418-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADEDLIFRL EGVDGGQSPR AGHDGDSDGD SDDEEGYFIC PITDDPSSNQ    50
    NVNSKVNKYY SNLTKSERYS SSGSPANSFH FKEAWKHAIQ KAKHMPDPWA 100
    EFHLEDIATE RATRHRYNAV TGEWLDDEVL IKMASQPFGR GAMRECFRTK 150
    KLSNFLHAQQ WKGASNYVAK RYIEPVDRDV YFEDVRLQME AKLWGEEYNR 200
    HKPPKQVDIM QMCIIELKDR PGKPLFHLEH YIEGKYIKYN SNSGFVRDDN 250
    IRLTPQAFSH FTFERSGHQL IVVDIQGVGD LYTDPQIHTE TGTDFGDGNL 300
    GVRGMALFFY SHACNRICES MGLAPFDLSP RERDAVNQNT KLLQSAKTIL 350
    RGTEEKCGSP QVRTLSGSRP PLLRPLSENS GDENMSDVTF DSLPSSPSSA 400
    TPHSQKLDHL HWPVFSDLDN MASRDHDHLD NHRESENSGD SGYPSEKRGE 450
    LDDPEPREHG HSYSNRKYES DEDSLGSSGR VCVEKWNLLN SSRLHLPRAS 500
    AVALEVQRLN ALDLEKKIGK SILGKVHLAM VRYHEGGRFC EKGEEWDQES 550
    AVFHLEHAAN LGELEAIVGL GLMYSQLPHH ILADVSLKET EENKTKGFDY 600
    LLKAAEAGDR QSMILVARAF DSGQNLSPDR CQDWLEALHW YNTALEMTDC 650
    DEGGEYDGMQ DEPRYMMLAR EAEMLFTGGY GLEKDPQRSG DLYTQAAEAA 700
    MEAMKGRLAN QYYQKAEEAW AQMEE 725
    Length:725
    Mass (Da):82,144
    Last modified:July 28, 2009 - v2
    Checksum:i9D2900E50EFF12DA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231H → R.2 Publications
    Corresponds to variant rs9935059 [ dbSNP | Ensembl ].
    VAR_033915
    Natural varianti75 – 751P → A.1 Publication
    Corresponds to variant rs17841292 [ dbSNP | Ensembl ].
    VAR_033916
    Natural varianti291 – 2911T → M in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041534
    Natural varianti361 – 3611Q → R.2 Publications
    Corresponds to variant rs4783453 [ dbSNP | Ensembl ].
    VAR_058405
    Natural varianti433 – 4331R → W.1 Publication
    Corresponds to variant rs56137739 [ dbSNP | Ensembl ].
    VAR_041535
    Natural varianti609 – 6091D → H.1 Publication
    VAR_041536

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93850 mRNA. Translation: AAB58270.1.
    AC009034 Genomic DNA. No translation available.
    BC032665 mRNA. Translation: AAH32665.1.
    CCDSiCCDS10604.1.
    RefSeqiNP_037434.1. NM_013302.3.
    XP_005276554.1. XM_005276497.1.
    UniGeneiHs.498892.

    Genome annotation databases

    EnsembliENST00000263026; ENSP00000263026; ENSG00000103319.
    GeneIDi101930123.
    29904.
    KEGGihsa:101930123.
    hsa:29904.
    UCSCiuc002dki.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U93850 mRNA. Translation: AAB58270.1 .
    AC009034 Genomic DNA. No translation available.
    BC032665 mRNA. Translation: AAH32665.1 .
    CCDSi CCDS10604.1.
    RefSeqi NP_037434.1. NM_013302.3.
    XP_005276554.1. XM_005276497.1.
    UniGenei Hs.498892.

    3D structure databases

    ProteinModelPortali O00418.
    SMRi O00418. Positions 117-323, 527-645.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118953. 33 interactions.
    IntActi O00418. 10 interactions.
    MINTi MINT-207181.
    STRINGi 9606.ENSP00000263026.

    Chemistry

    BindingDBi O00418.
    ChEMBLi CHEMBL5026.
    GuidetoPHARMACOLOGYi 2014.

    PTM databases

    PhosphoSitei O00418.

    Proteomic databases

    MaxQBi O00418.
    PaxDbi O00418.
    PRIDEi O00418.

    Protocols and materials databases

    DNASUi 29904.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263026 ; ENSP00000263026 ; ENSG00000103319 .
    GeneIDi 101930123.
    29904.
    KEGGi hsa:101930123.
    hsa:29904.
    UCSCi uc002dki.3. human.

    Organism-specific databases

    CTDi 29904.
    GeneCardsi GC16P022217.
    HGNCi HGNC:24615. EEF2K.
    HPAi CAB007818.
    MIMi 606968. gene.
    neXtProti NX_O00418.
    PharmGKBi PA134992891.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG145133.
    HOGENOMi HOG000022023.
    HOVERGENi HBG002318.
    InParanoidi O00418.
    KOi K08292.
    OMAi QIHTETG.
    OrthoDBi EOG7673B0.
    PhylomeDBi O00418.
    TreeFami TF316085.

    Enzyme and pathway databases

    BRENDAi 2.7.11.20. 2681.
    Reactomei REACT_6772. S6K1 signalling.

    Miscellaneous databases

    GeneWikii EEF2K.
    NextBioi 52478.
    PROi O00418.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00418.
    Bgeei O00418.
    CleanExi HS_EEF2K.
    Genevestigatori O00418.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    InterProi IPR017400. Elongation_factor_2_kinase.
    IPR011009. Kinase-like_dom.
    IPR004166. MHCK_EF2_kinase.
    IPR006597. Sel1-like.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF02816. Alpha_kinase. 1 hit.
    PF08238. Sel1. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF038139. Elongation_factor_2_kinase. 1 hit.
    SMARTi SM00811. Alpha_kinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51158. ALPHA_KINASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, VARIANT ARG-361.
      Tissue: Glial tumor.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-23 AND ARG-361.
      Tissue: Lymph.
    4. "Mapping the functional domains of elongation factor-2 kinase."
      Pavur K.S., Petrov A.N., Ryazanov A.G.
      Biochemistry 39:12216-12224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION, DOMAIN.
    5. "A novel method to identify protein kinase substrates: eEF2 kinase is phosphorylated and inhibited by SAPK4/p38delta."
      Knebel A., Morrice N., Cohen P.
      EMBO J. 20:4360-4369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-359.
    6. "Regulation of elongation factor 2 kinase by p90(RSK1) and p70 S6 kinase."
      Wang X., Li W., Williams M., Terada N., Alessi D.R., Proud C.G.
      EMBO J. 20:4370-4379(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-366 BY RPS6KA1 AND RPS6KB1, MUTAGENESIS OF SER-366.
    7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Stimulation of the AMP-activated protein kinase leads to activation of eukaryotic elongation factor 2 kinase and to its phosphorylation at a novel site, serine 398."
      Browne G.J., Finn S.G., Proud C.G.
      J. Biol. Chem. 279:12220-12231(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-398.
    9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "cdc2-cyclin B regulates eEF2 kinase activity in a cell cycle- and amino acid-dependent manner."
      Smith E.M., Proud C.G.
      EMBO J. 27:1005-1016(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-359.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-348; SER-470; SER-474 AND SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-348; SER-445; SER-470 AND SER-474, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "The channel-kinase TRPM7 regulates phosphorylation of the translational factor eEF2 via eEF2-k."
      Perraud A.L., Zhao X., Ryazanov A.G., Schmitz C.
      Cell. Signal. 23:586-593(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-78.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18 AND SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Identification of autophosphorylation sites in eukaryotic elongation factor-2 kinase."
      Pyr Dit Ruys S., Wang X., Smith E.M., Herinckx G., Hussain N., Rider M.H., Vertommen D., Proud C.G.
      Biochem. J. 442:681-692(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-61; SER-66; SER-78; THR-348; THR-353; SER-366; SER-445; SER-474 AND SER-491, MUTAGENESIS OF SER-78; THR-348 AND SER-366.
    20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    21. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ARG-23; ALA-75; MET-291; TRP-433 AND HIS-609.

    Entry informationi

    Entry nameiEF2K_HUMAN
    AccessioniPrimary (citable) accession number: O00418
    Secondary accession number(s): Q8N588
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: July 28, 2009
    Last modified: October 1, 2014
    This is version 139 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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